| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-128 |
Sentence |
denotes |
Amyloid-beta interactions with chondroitin sulfate-derived monosaccharides and disaccharides. implications for drug development. |
| T2 |
129-281 |
Sentence |
denotes |
In Alzheimer's disease, the major pathological features are diffuse and senile plaques that are primarily composed of the amyloid-beta (A beta) peptide. |
| T3 |
282-426 |
Sentence |
denotes |
It has been proposed that proteoglycans and glycosaminoglycans (GAG) facilitate amyloid fibril formation and/or stabilize the plaque aggregates. |
| T4 |
427-565 |
Sentence |
denotes |
To develop effective therapeutics based on A beta-GAG interactions, understanding the A beta binding motif on the GAG chain is imperative. |
| T5 |
566-835 |
Sentence |
denotes |
Using electron microscopy, fluorescence spectroscopy, and competitive inhibition ELISAs, we have evaluated the ability of chondroitin sulfate-derived monosaccharides and disaccharides to induce the structural changes in A beta that are associated with GAG interactions. |
| T6 |
836-1190 |
Sentence |
denotes |
Our results demonstrate that the disaccharides GalNAc-4-sulfate(4S), Delta UA-GalNAc-6-sulfate(6S), and Delta UA-GalNAc-4,6-sulfate(4S,6S), the iduronic acid-2-sulfate analogues, and the monosaccharides d-GalNAc-4S, d-GalNAc-6S, and d-GalNAc-4S,6S, but not d-GalNAc, d-GlcNAc, or Delta UA-GalNAc, induce the fibrillar features of A beta-GAG interactions. |
| T7 |
1191-1298 |
Sentence |
denotes |
The binding affinities of all chondroitin sulfate-derived saccharides mimic those of the intact GAG chains. |
| T8 |
1299-1475 |
Sentence |
denotes |
The sulfated monosaccharides and disaccharides compete with the intact chondroitin sulfate and heparin GAGs for A beta binding, as illustrated by competitive inhibition ELISAs. |
| T9 |
1476-1672 |
Sentence |
denotes |
Therefore, the development of therapeutics based on the model of A beta-chondroitin sulfate binding may lead to effective inhibitors of the GAG-induced amyloid formation that is observed in vitro. |